Protein-Protein Interactions of Tandem Affinity Purified Protein Kinases from Rice

نویسندگان

  • Jai S. Rohila
  • Mei Chen
  • Shuo Chen
  • Johann Chen
  • Ronald L. Cerny
  • Christopher Dardick
  • Patrick Canlas
  • Hiroaki Fujii
  • Michael Gribskov
  • Siddhartha Kanrar
  • Lucas Knoflicek
  • Becky Stevenson
  • Mingtang Xie
  • Xia Xu
  • Xianwu Zheng
  • Jian-Kang Zhu
  • Pamela Ronald
  • Michael E. Fromm
چکیده

Eighty-eight rice (Oryza sativa) cDNAs encoding rice leaf expressed protein kinases (PKs) were fused to a Tandem Affinity Purification tag (TAP-tag) and expressed in transgenic rice plants. The TAP-tagged PKs and interacting proteins were purified from the T1 progeny of the transgenic rice plants and identified by tandem mass spectrometry. Forty-five TAP-tagged PKs were recovered in this study and thirteen of these were found to interact with other rice proteins with a high probability score. In vivo phosphorylated sites were found for three of the PKs. A comparison of the TAP-tagged data from a combined analysis of 129 TAP-tagged rice protein kinases with a concurrent screen using yeast two hybrid methods identified an evolutionarily new rice protein that interacts with the well conserved cell division cycle 2 (CDC2) protein complex.

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عنوان ژورنال:

دوره 4  شماره 

صفحات  -

تاریخ انتشار 2009